title: Secretion of tyrosinase in Streptomyces glaucescens.
abstract: In Streptomyces glaucescens, the intracellular and the extracellular enzyme forms of tyrosinase were found to be indentical in molecular weight (29 000), in copper content (0.21%), in the 19 amino acids at the amino-terminal end and in the ratio of cresolase to catecholase activity (0,005). The tyrosinase secretion process exhibited a constant rate of 0.15 units h-1 (mg protein)-1. Under highly induced conditions intracellular tyrosinase was accumulated. Mutations responsible for the non-melanogenic, tyrosinase-positive non-secretor mutant type are located chromosomally on the upper right arc of the S. glaucescens map near the ade-1 marker.
mesh_terms: D004156:Catechol Oxidase / Q000378:metabolism*; D002874:Chromosome Mapping; D002876:Chromosomes, Bacterial; D003300:Copper / Q000032:analysis; D007700:Kinetics; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000032:analysis / Q000378:metabolism*; D009154:Mutation; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics
chemical_list: D003300:Copper; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase